Fluorine in PDB 2k1q: uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor

The structure of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor also contains other interesting chemical elements:

Chlorine	(Cl)	20 atoms
Zinc	(Zn)	20 atoms

The binding sites of Fluorine atom in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor (pdb code 2k1q). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor, PDB code: 2k1q:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:F190 b:0.0 occ:1.00 FG1 B:OBF190 0.0 0.0 1.0 CG B:OBF190 1.3 0.0 1.0 HG B:OBF190 2.0 0.0 1.0 FG2 B:OBF190 2.2 0.0 1.0 CB B:OBF190 2.4 0.0 1.0 H1B B:OBF190 2.5 0.0 1.0 HB3 A:LEU135 2.6 0.0 1.0 HA A:LYS136 2.6 0.0 1.0 H2B B:OBF190 2.9 0.0 1.0 HE2 A:PHE154 3.0 0.0 1.0 O A:LEU135 3.1 0.0 1.0 C A:LEU135 3.1 0.0 1.0 HG2 A:LYS136 3.2 0.0 1.0 N A:LYS136 3.2 0.0 1.0 HB3 A:ALA157 3.3 0.0 1.0 CA A:LYS136 3.3 0.0 1.0 HD3 A:LYS136 3.4 0.0 1.0 HZ A:PHE154 3.5 0.0 1.0 CB A:LEU135 3.5 0.0 1.0 CA B:OBF190 3.6 0.0 1.0 HD2 A:LYS136 3.7 0.0 1.0 HA B:OBF190 3.7 0.0 1.0 H A:LYS136 3.7 0.0 1.0 CD A:LYS136 3.8 0.0 1.0 HB2 A:LEU135 3.9 0.0 1.0 CE2 A:PHE154 3.9 0.0 1.0 CG A:LYS136 3.9 0.0 1.0 CA A:LEU135 3.9 0.0 1.0 O A:VAL132 4.1 0.0 1.0 HB1 A:ALA157 4.1 0.0 1.0 CZ A:PHE154 4.1 0.0 1.0 CB A:ALA157 4.2 0.0 1.0 N B:OBF190 4.3 0.0 1.0 CB A:LYS136 4.3 0.0 1.0 H A:ALA157 4.3 0.0 1.0 H A:GLY137 4.4 0.0 1.0 C A:LYS136 4.5 0.0 1.0 H A:SER138 4.5 0.0 1.0 OG A:SER138 4.5 0.0 1.0 O B:LEU189 4.7 0.0 1.0 HG A:SER138 4.7 0.0 1.0 HN B:OBF190 4.7 0.0 1.0 C B:LEU189 4.7 0.0 1.0 CG A:LEU135 4.7 0.0 1.0 HA A:LEU135 4.7 0.0 1.0 HD22 A:LEU135 4.7 0.0 1.0 HB2 A:ALA157 4.8 0.0 1.0 HG2 B:GLU188 4.8 0.0 1.0 O B:GLU188 4.8 0.0 1.0 HD21 A:LEU135 4.8 0.0 1.0 N A:GLY137 4.8 0.0 1.0 C B:OBF190 4.8 0.0 1.0 HG A:LEU135 4.8 0.0 1.0 N A:ALA157 4.8 0.0 1.0 N A:LEU135 4.8 0.0 1.0 HA A:ALA156 4.9 0.0 1.0 HG3 A:LYS136 4.9 0.0 1.0 H A:LEU135 4.9 0.0 1.0 HB2 A:LYS136 4.9 0.0 1.0 O B:OBF190 4.9 0.0 1.0 HB3 A:LYS136 5.0 0.0 1.0

Fluorine binding site 2 out of 2 in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:F190 b:0.0 occ:1.00 FG2 B:OBF190 0.0 0.0 1.0 CG B:OBF190 1.4 0.0 1.0 HG B:OBF190 2.0 0.0 1.0 FG1 B:OBF190 2.2 0.0 1.0 CB B:OBF190 2.4 0.0 1.0 H2B B:OBF190 2.5 0.0 1.0 H A:ALA157 2.6 0.0 1.0 O B:GLU188 2.7 0.0 1.0 HB3 A:ALA157 2.8 0.0 1.0 HA A:ALA156 2.9 0.0 1.0 N B:OBF190 2.9 0.0 1.0 C B:LEU189 3.2 0.0 1.0 CA B:OBF190 3.2 0.0 1.0 HZ A:PHE154 3.2 0.0 1.0 HN B:OBF190 3.2 0.0 1.0 H1B B:OBF190 3.2 0.0 1.0 N A:ALA157 3.3 0.0 1.0 HE2 A:PHE154 3.4 0.0 1.0 HA B:OBF190 3.5 0.0 1.0 O B:LEU189 3.5 0.0 1.0 C B:GLU188 3.6 0.0 1.0 HG2 B:GLU188 3.7 0.0 1.0 CB A:ALA157 3.7 0.0 1.0 HA B:LEU189 3.8 0.0 1.0 CZ A:PHE154 3.8 0.0 1.0 CA A:ALA156 3.8 0.0 1.0 CA B:LEU189 3.9 0.0 1.0 CE2 A:PHE154 3.9 0.0 1.0 HD3 A:LYS136 3.9 0.0 1.0 HB3 B:GLU188 3.9 0.0 1.0 C A:ALA156 3.9 0.0 1.0 HB1 A:ALA157 4.0 0.0 1.0 N B:LEU189 4.1 0.0 1.0 CA A:ALA157 4.2 0.0 1.0 HB3 A:LEU135 4.2 0.0 1.0 HA A:LYS136 4.3 0.0 1.0 CG B:GLU188 4.5 0.0 1.0 CB B:GLU188 4.5 0.0 1.0 HB2 A:ALA157 4.5 0.0 1.0 C B:OBF190 4.5 0.0 1.0 HD2 A:LYS136 4.6 0.0 1.0 HB2 A:SER139 4.6 0.0 1.0 HB3 A:ALA156 4.6 0.0 1.0 CA B:GLU188 4.7 0.0 1.0 CB A:ALA156 4.7 0.0 1.0 CD A:LYS136 4.7 0.0 1.0 O A:ARG155 4.7 0.0 1.0 HB2 A:ALA156 4.7 0.0 1.0 HG2 A:LYS136 4.8 0.0 1.0 OE1 B:GLU188 4.8 0.0 1.0 N A:ALA156 4.9 0.0 1.0 CE1 A:PHE154 4.9 0.0 1.0 HA A:ALA157 5.0 0.0 1.0 H B:GLU188 5.0 0.0 1.0 H B:LEU189 5.0 0.0 1.0 O A:ALA156 5.0 0.0 1.0

M.Gallo, M.Pennestri, M.J.Bottomley, G.Barbato, T.Eliseo, M.Paci, F.Narjes, R.De Francesco, V.Summa, U.Koch, R.Bazzo, D.O.Cicero. Binding of A Noncovalent Inhibitor Exploiting the S' Region Stabilizes the Hepatitis C Virus NS3 Protease Conformation in the Absence of Cofactor. J.Mol.Biol. V. 385 1142 2009.
ISSN: ISSN 0022-2836
PubMed: 19061898
DOI: 10.1016/J.JMB.2008.11.017